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Matches in Nanopublications for { ?s ?p "Furthermore, serum starvation-induced apoptosis caused a twofold increase in caspase 3 activity in C1-TEN-overexpressing cells vs. mock cells. In addition, C1-TEN-overexpressing cells showed a markedly reduced phosphorylation of Akt/PKB kinase and its substrate GSK3, as well as reduced Akt enzymatic activity. Equal amounts of total cell lysates were subjected to 10% SDSPAGE. The membrane was then probed with polyclonal antibody against GSK3 specifically phosphorylated at Ser21/9 (pGSK3?/?, CST), after which the membrane was stripped (stripping buffer, Pierce) and reprobed with polyclonal anti-total Akt antibody (CST). and Western blotting for detection of either Akt kinase specifically phosphorylated at Ser473 (pAkt) or both 42 and 44 kDa isoforms of phosphorylated ERK (pERK) using specific antibodies (Santa Cruz Biotechnology, Santa Cruz, CA)." ?g. }

• _5 value "Furthermore, serum starvation-induced apoptosis caused a twofold increase in caspase 3 activity in C1-TEN-overexpressing cells vs. mock cells. In addition, C1-TEN-overexpressing cells showed a markedly reduced phosphorylation of Akt/PKB kinase and its substrate GSK3, as well as reduced Akt enzymatic activity. Equal amounts of total cell lysates were subjected to 10% SDSPAGE. The membrane was then probed with polyclonal antibody against GSK3 specifically phosphorylated at Ser21/9 (pGSK3?/?, CST), after which the membrane was stripped (stripping buffer, Pierce) and reprobed with polyclonal anti-total Akt antibody (CST). and Western blotting for detection of either Akt kinase specifically phosphorylated at Ser473 (pAkt) or both 42 and 44 kDa isoforms of phosphorylated ERK (pERK) using specific antibodies (Santa Cruz Biotechnology, Santa Cruz, CA)." provenance.
• _5 value "Furthermore, serum starvation-induced apoptosis caused a twofold increase in caspase 3 activity in C1-TEN-overexpressing cells vs. mock cells. In addition, C1-TEN-overexpressing cells showed a markedly reduced phosphorylation of Akt/PKB kinase and its substrate GSK3, as well as reduced Akt enzymatic activity. Equal amounts of total cell lysates were subjected to 10% SDSPAGE. The membrane was then probed with polyclonal antibody against GSK3 specifically phosphorylated at Ser21/9 (pGSK3?/?, CST), after which the membrane was stripped (stripping buffer, Pierce) and reprobed with polyclonal anti-total Akt antibody (CST). and Western blotting for detection of either Akt kinase specifically phosphorylated at Ser473 (pAkt) or both 42 and 44 kDa isoforms of phosphorylated ERK (pERK) using specific antibodies (Santa Cruz Biotechnology, Santa Cruz, CA)." provenance.
• _5 value "Furthermore, serum starvation-induced apoptosis caused a twofold increase in caspase 3 activity in C1-TEN-overexpressing cells vs. mock cells. In addition, C1-TEN-overexpressing cells showed a markedly reduced phosphorylation of Akt/PKB kinase and its substrate GSK3, as well as reduced Akt enzymatic activity. Equal amounts of total cell lysates were subjected to 10% SDSPAGE. The membrane was then probed with polyclonal antibody against GSK3 specifically phosphorylated at Ser21/9 (pGSK3?/?, CST), after which the membrane was stripped (stripping buffer, Pierce) and reprobed with polyclonal anti-total Akt antibody (CST). and Western blotting for detection of either Akt kinase specifically phosphorylated at Ser473 (pAkt) or both 42 and 44 kDa isoforms of phosphorylated ERK (pERK) using specific antibodies (Santa Cruz Biotechnology, Santa Cruz, CA)." provenance.
• _2 value "Furthermore, serum starvation-induced apoptosis caused a twofold increase in caspase 3 activity in C1-TEN-overexpressing cells vs. mock cells. In addition, C1-TEN-overexpressing cells showed a markedly reduced phosphorylation of Akt/PKB kinase and its substrate GSK3, as well as reduced Akt enzymatic activity. Equal amounts of total cell lysates were subjected to 10% SDSPAGE. The membrane was then probed with polyclonal antibody against GSK3 specifically phosphorylated at Ser21/9 (pGSK3?/?, CST), after which the membrane was stripped (stripping buffer, Pierce) and reprobed with polyclonal anti-total Akt antibody (CST). and Western blotting for detection of either Akt kinase specifically phosphorylated at Ser473 (pAkt) or both 42 and 44 kDa isoforms of phosphorylated ERK (pERK) using specific antibodies (Santa Cruz Biotechnology, Santa Cruz, CA)." provenance.
• _2 value "Furthermore, serum starvation-induced apoptosis caused a twofold increase in caspase 3 activity in C1-TEN-overexpressing cells vs. mock cells. In addition, C1-TEN-overexpressing cells showed a markedly reduced phosphorylation of Akt/PKB kinase and its substrate GSK3, as well as reduced Akt enzymatic activity. Equal amounts of total cell lysates were subjected to 10% SDSPAGE. The membrane was then probed with polyclonal antibody against GSK3 specifically phosphorylated at Ser21/9 (pGSK3?/?, CST), after which the membrane was stripped (stripping buffer, Pierce) and reprobed with polyclonal anti-total Akt antibody (CST). and Western blotting for detection of either Akt kinase specifically phosphorylated at Ser473 (pAkt) or both 42 and 44 kDa isoforms of phosphorylated ERK (pERK) using specific antibodies (Santa Cruz Biotechnology, Santa Cruz, CA)." provenance.
• _5 value "Furthermore, serum starvation-induced apoptosis caused a twofold increase in caspase 3 activity in C1-TEN-overexpressing cells vs. mock cells. In addition, C1-TEN-overexpressing cells showed a markedly reduced phosphorylation of Akt/PKB kinase and its substrate GSK3, as well as reduced Akt enzymatic activity. Equal amounts of total cell lysates were subjected to 10% SDSPAGE. The membrane was then probed with polyclonal antibody against GSK3 specifically phosphorylated at Ser21/9 (pGSK3?/?, CST), after which the membrane was stripped (stripping buffer, Pierce) and reprobed with polyclonal anti-total Akt antibody (CST). and Western blotting for detection of either Akt kinase specifically phosphorylated at Ser473 (pAkt) or both 42 and 44 kDa isoforms of phosphorylated ERK (pERK) using specific antibodies (Santa Cruz Biotechnology, Santa Cruz, CA)." provenance.